Inactivation of yeast hexokinase by 2-aminothiophenol. Evidence for a ‘half-of-the-sites’ mechanism
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چکیده
منابع مشابه
Inactivation of yeast hexokinase by 2-aminothiophenol. Evidence for a 'half-of-the-sites' mechanism.
Yeast hexokinase is a homodimer consisting of two identical subunits. Yeast hexokinase was inactivated by 2-aminothiophenol at 25 degrees C (pH 9.1). The reaction followed pseudo-first-order kinetics until about 70% of the phosphotransferase activity was lost. About 0.65 mol of 2-aminothiophenol/mol of hexokinase was found to be bound after the 70% loss of the enzyme activity. Completely inacti...
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15 صفحه اولReversible inactivation and dissociation of yeast hexokinase.
Recent’ work on the reactivation and reconstitution of several denatured enzymes has provided increasing understanding of the process of reversible protein denaturation. Studies on ribonuclease by Anfinsen et al. (1) and White (2) have convincingly demonstrated that under favorable conditions a complet,ely denatured protein can resume the active three-dimensional configuration of the native mol...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1988
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2540819